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208 related items for PubMed ID: 7686901
1. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure. Reddy GL, Iwamoto T, Tomich JM, Montal M. J Biol Chem; 1993 Jul 15; 268(20):14608-15. PubMed ID: 7686901 [Abstract] [Full Text] [Related]
5. Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. Montal MO, Iwamoto T, Tomich JM, Montal M. FEBS Lett; 1993 Apr 12; 320(3):261-6. PubMed ID: 7681786 [Abstract] [Full Text] [Related]
6. Free energy analysis of conductivity and charge selectivity of M2GlyR-derived synthetic channels. Chen J, Tomich JM. Biochim Biophys Acta; 2014 Sep 12; 1838(9):2319-25. PubMed ID: 24582709 [Abstract] [Full Text] [Related]
16. Mechanism for the channel-opening reaction of strychnine-sensitive glycine receptors on cultured embryonic mouse spinal cord cells. Walstrom KM, Hess GP. Biochemistry; 1994 Jun 21; 33(24):7718-30. PubMed ID: 7516705 [Abstract] [Full Text] [Related]
17. M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Oiki S, Danho W, Madison V, Montal M. Proc Natl Acad Sci U S A; 1988 Nov 21; 85(22):8703-7. PubMed ID: 2460876 [Abstract] [Full Text] [Related]
18. Emerging issues of connexin channels: biophysics fills the gap. Harris AL. Q Rev Biophys; 2001 Aug 21; 34(3):325-472. PubMed ID: 11838236 [Abstract] [Full Text] [Related]
20. Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels. Iwamoto T, Grove A, Montal MO, Montal M, Tomich JM. Int J Pept Protein Res; 1994 Jun 21; 43(6):597-607. PubMed ID: 7523324 [Abstract] [Full Text] [Related] Page: [Next] [New Search]